Co-operative domains in fibronectin.
The melting of human plasma fibronectin and its proteolytic fragments has been studied by scanning microcalorimetry to reveal co-operative structural domains in the molecule. It has been established that each of the two similar polypeptide chains of fibronectin has at least 12 structural domains, which differ in stability, size and function. Many of the domains in the N-terminal half of the polypeptide chains appear to be composed of two homologous repeat modules that co-operate to form a single co-operative unit. In the intact fibronectin molecule, the C-terminal regions of both chains seem to interact forming a stable co-operative block.
Tatunashvili
L V
LV
Institute of Protein Research, Academy of Sciences of the U.S.S.R., Pushchino, Moscow Region.
Filimonov
V V
VV
Privalov
P L
PL
Metsis
M L
ML
Koteliansky
V E
VE
Ingham
K C
KC
Medved
L V
LV
D002152:Calorimetry, Differential Scanning; D005353:Fibronectins / Q000097:blood*; D006493:Heparin / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008961:Models, Structural; D008970:Molecular Weight; D010446:Peptide Fragments; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation
D005353:Fibronectins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D006493:Heparin